SitesBLAST
Comparing WP_068862274.1 NCBI__GCF_001677335.1:WP_068862274.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
46% identity, 99% coverage: 6:535/535 of query aligns to 2:539/539 of P0DX84
- H231 (= H227) mutation to A: Retains 74% of wild-type activity.
- W235 (= W231) mutation to A: Almost completely abolishes the activity.
- G302 (= G297) mutation to P: Almost completely abolishes the activity.
- G303 (= G298) mutation to P: Almost completely abolishes the activity.
- W326 (= W320) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P327) mutation to A: Retains 69% of wild-type activity.
- R432 (= R428) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K430) mutation to A: Retains 36% of wild-type activity.
- D435 (= D431) mutation to A: Retains 76% of wild-type activity.
- K438 (= K434) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G436) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G437) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E438) mutation to A: Retains 27% of wild-type activity.
- W443 (= W439) mutation to A: Retains 60% of wild-type activity.
- E474 (= E470) mutation to A: Retains 33% of wild-type activity.
- K523 (= K519) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K522) mutation to A: Retains 48% of wild-type activity.
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
46% identity, 98% coverage: 6:531/535 of query aligns to 2:535/538 of 6ijbB
- active site: T185 (= T181), H205 (= H201), H231 (= H227), S329 (≠ T323), E330 (= E324), K438 (= K434), W443 (= W439), A523 (≠ K519)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W231), G303 (= G298), A325 (= A319), W326 (= W320), G327 (= G321), M328 (= M322)
- binding adenosine monophosphate: G303 (= G298), A304 (≠ S299), A305 (= A300), H324 (= H318), W326 (= W320), G327 (= G321), M328 (= M322), S329 (≠ T323), Q359 (= Q353), D417 (= D413)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
45% identity, 98% coverage: 6:531/535 of query aligns to 2:532/533 of 6ihkB
- active site: T185 (= T181), H202 (= H201), H228 (= H227), S326 (≠ T323), E327 (= E324), K435 (= K434), W440 (= W439), K520 (= K519)
- binding adenosine-5'-diphosphate: H228 (= H227), G300 (= G298), A301 (≠ S299), A302 (= A300), H321 (= H318), A322 (= A319), W323 (= W320), G324 (= G321), M325 (= M322), S326 (≠ T323), Q356 (= Q353), D414 (= D413), R429 (= R428), K520 (= K519)
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
43% identity, 98% coverage: 9:532/535 of query aligns to 13:537/541 of Q5SKN9
- T184 (= T181) binding Mg(2+)
- G302 (= G298) binding tetradecanoyl-AMP
- Q322 (≠ H318) binding tetradecanoyl-AMP
- G323 (≠ A319) binding tetradecanoyl-AMP
- T327 (= T323) binding tetradecanoyl-AMP
- E328 (= E324) binding Mg(2+)
- D418 (= D413) binding tetradecanoyl-AMP
- K435 (= K430) binding tetradecanoyl-AMP
- K439 (= K434) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 98% coverage: 9:532/535 of query aligns to 6:506/510 of 1v26B
- active site: T177 (= T181), H197 (= H201), H223 (= H227), T320 (= T323), E321 (= E324), K432 (= K434), W437 (= W439)
- binding adenosine monophosphate: G295 (= G298), S296 (= S299), A297 (= A300), G316 (≠ A319), Y317 (≠ W320), G318 (= G321), L319 (≠ M322), T320 (= T323), D411 (= D413), K428 (= K430), K432 (= K434), W437 (= W439)
- binding magnesium ion: T177 (= T181), E321 (= E324)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
39% identity, 98% coverage: 9:532/535 of query aligns to 6:487/491 of 1v25A
- active site: T177 (= T181), H197 (= H201), H223 (= H227), T320 (= T323), E321 (= E324), K432 (= K434), W437 (= W439)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H227), V224 (≠ A228), G295 (= G298), S296 (= S299), A297 (= A300), Y317 (≠ W320), G318 (= G321), L319 (≠ M322), T320 (= T323), D411 (= D413), I423 (≠ L425), K432 (= K434), W437 (= W439)
- binding magnesium ion: T177 (= T181), E321 (= E324)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
34% identity, 93% coverage: 29:526/535 of query aligns to 25:526/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G297), G293 (= G298), A294 (≠ S299), A295 (= A300), G314 (≠ A319), Y315 (≠ W320), M317 (= M322), S318 (≠ T323), D408 (= D413), R423 (= R428)
- binding 4'-phosphopantetheine: R93 (= R101), P220 (= P224), H223 (= H227)
8i49A Acyl-acp synthetase structure bound to atp
34% identity, 93% coverage: 29:526/535 of query aligns to 25:526/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
34% identity, 93% coverage: 29:526/535 of query aligns to 25:526/530 of 8i22A